ID A0A0A0EH76_9RHOB Unreviewed; 387 AA.
AC A0A0A0EH76;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Isovaleryl-CoA dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00018258};
DE EC=1.3.8.4 {ECO:0000256|ARBA:ARBA00012044};
GN ORFNames=ATO9_13060 {ECO:0000313|EMBL:KGM48552.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM48552.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM48552.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM48552.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = 3-methyl-(2E)-butenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:12276, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:57345, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307; EC=1.3.8.4;
CC Evidence={ECO:0000256|ARBA:ARBA00023730};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR634183-3, ECO:0000256|RuleBase:RU362125};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004898}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGM48552.1}.
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DR EMBL; AQQX01000004; KGM48552.1; -; Genomic_DNA.
DR RefSeq; WP_043749466.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EH76; -.
DR STRING; 1461694.ATO9_13060; -.
DR eggNOG; COG1960; Bacteria.
DR OrthoDB; 9775090at2; -.
DR Proteomes; UP000030004; Unassembled WGS sequence.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IEA:UniProt.
DR CDD; cd01156; IVD; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR034183; IVD.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 2.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR634183-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000030004}.
FT DOMAIN 12..123
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 127..222
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 234..382
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-1"
FT BINDING 128..137
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 161..163
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 183..184
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 245..248
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 273
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 341..345
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
FT BINDING 368..369
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-2"
FT BINDING 370..372
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR634183-3"
SQ SEQUENCE 387 AA; 41994 MW; 988AE6E90D51C0D8 CRC64;
MFNASMTFDL GEDVNALRDM VHRFAQERIK PQAAEIDSSN EFPPALWREM GDLGLLGITV
DEAYGGSGMS YLAHVIAVEE IARASASVSL SYGAHSNLCV NQIKLNGSEE QKQKYLPGLI
SGEHVGALAM SEPSAGSDVV SMKLKAEKRN GYYVLNGNKY WITNGPDADT LVVYAKTDPE
AGSKGITAFI IEKDMTGFST SPHFDKLGMR GSNTAELIFD NCEVPFENVL GEEGKGVRVL
MSGLDYERVV LSGIGTGIMA ACLDEIMPYM VERKQFGQSI GNFQLMQGKI ADMYTKMNSA
RAYVYEVAKA CDRGEVTRQD AAACVLYASE EAMVVAHQAV QAMGGAGYLN DNPVGRIFRD
AKLMEIGAGT SEIRRMLIGR ELMASMS
//
